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- W2367049757 abstract "Chaperone can facilitate the nascent peptide and denatured protein to fold to the native state but do not occur in these structures when the structures are performing their normal biological functions.Peptides need the help of chaperones to fold to the nature state when they are produced from the ribosomes.Protein ObgE from E.coli is a highly conserved GTPase.ObgE participates in cell signaling,transportation of protein and cell cycle regulation.In present work,we cloned the DNA of E.coli ObgE into vector pET-28a,expressed in E.coli BL21,and then purified the protein.After the purification of ObgE,we tested its chaperone activity by using renaturation of citrate synthase,α-glucosidase and bovine carbonic anhydrase Ⅱ.We found that ObgE has chaperone activity to a certain extent.This result will have impact on the research of protein ObgE." @default.
- W2367049757 created "2016-06-24" @default.
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- W2367049757 date "2011-01-01" @default.
- W2367049757 modified "2023-09-23" @default.
- W2367049757 title "Chaperone Activity of Conservative GTPase ObgE" @default.
- W2367049757 hasPublicationYear "2011" @default.
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